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MURA_HAEIN
ID   MURA_HAEIN              Reviewed;         424 AA.
AC   P45025;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000255|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000255|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000255|HAMAP-Rule:MF_00111}; Synonyms=murZ;
GN   OrderedLocusNames=HI_1081;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2] {ECO:0007744|PDB:3SWE}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP   ACTIVE SITE, AND FORMATION OF COVALENT REACTION INTERMEDIATE.
RX   PubMed=22378791; DOI=10.1074/jbc.m112.342725;
RA   Zhu J.Y., Yang Y., Han H., Betzi S., Olesen S.H., Marsilio F.,
RA   Schoenbrunn E.;
RT   "Functional consequence of covalent reaction of phosphoenolpyruvate with
RT   UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA).";
RL   J. Biol. Chem. 287:12657-12667(2012).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000255|HAMAP-Rule:MF_00111}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine =
CC         phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:18681, ChEBI:CHEBI:43474, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58702, ChEBI:CHEBI:68483; EC=2.5.1.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00111};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00111}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00111}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00111}.
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DR   EMBL; L42023; AAC22737.1; -; Genomic_DNA.
DR   PIR; A64182; A64182.
DR   RefSeq; NP_439238.1; NC_000907.1.
DR   RefSeq; WP_005693405.1; NC_000907.1.
DR   PDB; 2RL1; X-ray; 2.20 A; A=1-424.
DR   PDB; 2RL2; X-ray; 2.30 A; A=1-424.
DR   PDB; 3SWE; X-ray; 2.20 A; A=1-424.
DR   PDBsum; 2RL1; -.
DR   PDBsum; 2RL2; -.
DR   PDBsum; 3SWE; -.
DR   AlphaFoldDB; P45025; -.
DR   SMR; P45025; -.
DR   STRING; 71421.HI_1081; -.
DR   EnsemblBacteria; AAC22737; AAC22737; HI_1081.
DR   KEGG; hin:HI_1081; -.
DR   PATRIC; fig|71421.8.peg.1126; -.
DR   eggNOG; COG0766; Bacteria.
DR   HOGENOM; CLU_027387_0_0_6; -.
DR   OMA; CDPHRAT; -.
DR   PhylomeDB; P45025; -.
DR   BioCyc; HINF71421:G1GJ1-1116-MON; -.
DR   BRENDA; 2.5.1.7; 2529.
DR   SABIO-RK; P45025; -.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; P45025; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00111; MurA; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR036968; Enolpyruvate_Tfrase_sf.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Peptidoglycan synthesis;
KW   Pyruvate; Reference proteome; Transferase.
FT   CHAIN           1..424
FT                   /note="UDP-N-acetylglucosamine 1-carboxyvinyltransferase"
FT                   /id="PRO_0000178876"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111,
FT                   ECO:0000305|PubMed:22378791"
FT   BINDING         22..23
FT                   /ligand="phosphoenolpyruvate"
FT                   /ligand_id="ChEBI:CHEBI:58702"
FT                   /evidence="ECO:0000305|PubMed:22378791,
FT                   ECO:0007744|PDB:3SWE"
FT   BINDING         93
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111"
FT   BINDING         122..126
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:22378791,
FT                   ECO:0007744|PDB:3SWE"
FT   BINDING         164..166
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:22378791,
FT                   ECO:0007744|PDB:3SWE"
FT   BINDING         307
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:22378791,
FT                   ECO:0007744|PDB:3SWE"
FT   BINDING         329
FT                   /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT                   /ligand_id="ChEBI:CHEBI:57705"
FT                   /evidence="ECO:0000269|PubMed:22378791,
FT                   ECO:0007744|PDB:3SWE"
FT   MOD_RES         117
FT                   /note="2-(S-cysteinyl)pyruvic acid O-phosphothioketal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00111,
FT                   ECO:0000305|PubMed:22378791"
FT   STRAND          2..8
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          14..17
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           22..31
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           32..34
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           48..58
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           93..98
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           99..106
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          107..112
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:2RL2"
FT   HELIX           125..133
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          137..141
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           165..175
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          178..185
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           191..201
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           234..245
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          250..255
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           258..260
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           262..270
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          274..277
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          279..285
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           306..308
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           309..317
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          319..326
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           336..341
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   TURN            342..344
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          346..350
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          353..357
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   TURN            372..375
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           376..384
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          385..392
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           395..400
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   HELIX           404..409
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   TURN            410..412
FT                   /evidence="ECO:0007829|PDB:2RL1"
FT   STRAND          415..419
FT                   /evidence="ECO:0007829|PDB:2RL1"
SQ   SEQUENCE   424 AA;  45187 MW;  EAB3170DF91F17C3 CRC64;
     MDKFRVYGQS RLSGSVNISG AKNAALPILF AAILATEPVK LTNVPELKDI ETTLKILRQL
     GVVVDRDATG AVLLDASNIN HFTAPYELVK TMRASIWALA PLVARFHQGQ VSLPGGCSIG
     ARPVDLHISG LEKLGADIVL EEGYVKAQVS DRLVGTRIVI EKVSVGATLS IMMAATLAKG
     TTVIENAARE PEIVDTADFL NKMGAKITGA GSAHITIEGV ERLTGCEHSV VPDRIETGTF
     LIAAAISGGC VVCQNTKADT LDAVIDKLRE AGAQVDVTEN SITLDMLGNR PKAVNIRTAP
     HPGFPTDMQA QFTLLNMVAE GTSIITETIF ENRFMHIPEL IRMGGKAEIE GNTAVCHGVE
     QLSGTEVIAT DLRASISLVL AGCIATGETI VDRIYHIDRG YEHIEDKLRG LGAKIERFSG
     SDEA
 
 
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